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Database: UniProt
Entry: A0A124GFF9_RHILI
LinkDB: A0A124GFF9_RHILI
Original site: A0A124GFF9_RHILI 
ID   A0A124GFF9_RHILI        Unreviewed;       547 AA.
AC   A0A124GFF9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Glucose-6-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=GPI {ECO:0000256|HAMAP-Rule:MF_00473};
DE            EC=5.3.1.9 {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphoglucose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PGI {ECO:0000256|HAMAP-Rule:MF_00473};
DE   AltName: Full=Phosphohexose isomerase {ECO:0000256|HAMAP-Rule:MF_00473};
DE            Short=PHI {ECO:0000256|HAMAP-Rule:MF_00473};
GN   Name=pgi {ECO:0000256|HAMAP-Rule:MF_00473};
GN   ORFNames=AU467_09140 {ECO:0000313|EMBL:KUM23508.1};
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381 {ECO:0000313|EMBL:KUM23508.1, ECO:0000313|Proteomes:UP000053176};
RN   [1] {ECO:0000313|EMBL:KUM23508.1, ECO:0000313|Proteomes:UP000053176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UFLA 01-765 {ECO:0000313|EMBL:KUM23508.1,
RC   ECO:0000313|Proteomes:UP000053176};
RA   Rangel W.M., Thijs S., Longatti S.M., Moreira F.M., Weyens N.,
RA   Vangronsveld J., Van Hamme J.D., Bottos E.M., Rineau F.;
RT   "Draft genome sequence of Mesorhizobium sp. UFLA 01-765, a multitolerant
RT   efficient symbiont and plant-growth promoting strain isolated from Zn-
RT   mining soil using Leucaena leucocephala as a trap plant.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible isomerization of glucose-6-phosphate
CC       to fructose-6-phosphate. {ECO:0000256|HAMAP-Rule:MF_00473}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC         Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC         EC=5.3.1.9; Evidence={ECO:0000256|ARBA:ARBA00029321,
CC         ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00473}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004926, ECO:0000256|HAMAP-Rule:MF_00473,
CC       ECO:0000256|RuleBase:RU000612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473}.
CC   -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|ARBA:ARBA00006604,
CC       ECO:0000256|HAMAP-Rule:MF_00473, ECO:0000256|RuleBase:RU000612}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KUM23508.1}.
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DR   EMBL; LPWA01000164; KUM23508.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124GFF9; -.
DR   OrthoDB; 140919at2; -.
DR   UniPathway; UPA00109; UER00181.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000053176; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR   GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901135; P:carbohydrate derivative metabolic process; IEA:InterPro.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05015; SIS_PGI_1; 1.
DR   CDD; cd05016; SIS_PGI_2; 1.
DR   Gene3D; 1.10.1390.10; -; 1.
DR   HAMAP; MF_00473; G6P_isomerase; 1.
DR   InterPro; IPR001672; G6P_Isomerase.
DR   InterPro; IPR023096; G6P_Isomerase_C.
DR   InterPro; IPR018189; Phosphoglucose_isomerase_CS.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   InterPro; IPR035476; SIS_PGI_1.
DR   InterPro; IPR035482; SIS_PGI_2.
DR   PANTHER; PTHR11469; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   PANTHER; PTHR11469:SF1; GLUCOSE-6-PHOSPHATE ISOMERASE; 1.
DR   Pfam; PF00342; PGI; 1.
DR   PRINTS; PR00662; G6PISOMERASE.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1.
DR   PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1.
DR   PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00473};
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00473};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00473}.
FT   ACT_SITE        350
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        381
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
FT   ACT_SITE        510
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00473"
SQ   SEQUENCE   547 AA;  59414 MW;  02663DF0106AEC93 CRC64;
     MDQSAFDKQL AALRDQRAAA KGTMREAFAA DPKRFERFSA TDGDLLLDWS KCAVDADTMA
     MLEKLAAAAD LAGRRAAMFE GKKINITENR AVLHTALRNL TGKGVVVDGQ DTKADVIAVL
     DAMGAFADDI RSGKAAGATG KKITDIVNIG IGGSDLGPAM VTLALAPYHD GPRAHYVSNV
     DGAHIHDTLK GLSPETTLFI IASKTFTTVE TMTNAETARK WVEKALGKEA IGKHFAAVST
     ALDLVAKFGI ASDRVFGFWD WVGGRYSVWS AIGLPVMIAI GPRNFRAFLD GAHEMDEHFR
     SAPLQKNLPV LLGLIGWWHR VVCKYPARAV IPYDQRLSRL PAYLQQLDME SNGKSVTLDG
     GAVTTPTGPL VWGEPGTNGQ HAFFQLLHQG TDFIPVEFLA AAVGHEPELK HQHDLLLANC
     LAQSEAFMKG RTLEEARTQM LAKGMKPADV DRIAPHRVFS GNRPSLTILY RKLDPRTLGR
     LIALYEHRVF VEGTLFNINS FDQWGVELGK ELATGLLPVV EGKETAAKRD ASTAGLVAYI
     HQLRGAE
//
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